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J. Biol. Chem., Vol. 281, Issue 20, 14376-14382, May 19, 2006

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Comparative Peptide Binding Studies of the PABC Domains from the Ubiquitin-protein Isopeptide Ligase HYD and Poly(A)-binding Protein

IMPLICATIONS FOR HYD FUNCTION^*

Nadia S. Lim¹, Guennadi Kozlov¹, Tsung-Cheng Chang, Olivia Groover, Nadeem Siddiqui, Laurent Volpon, Gregory De Crescenzo^¶, Ann-Bin Shyu, and Kalle Gehring, A Chercheur National of the Fonds de la Recherche en Santé de Québec²

From the Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montréal, Québec H3G 1Y6, Canada, the Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77030, and the ^¶Département de Génie Chimique, École Polytechnique de Montréal, 2500 chemin de Polytechnique, Montréal, Québec H3T 1J4, Canada

The PABC domain is a peptide-binding domain that is specifically found in poly(A)-binding protein (PABP) and a HECT ubiquitin-protein isopeptide ligase (E3) known as HYD (hyperplastic discs), EDD (E3 isolated by differential display), or Rat100. The PABC domain of PABP recruits various regulatory proteins and translation factors to poly(A) mRNAs through binding of a conserved 12-amino acid peptide motif, PAM2 (PABP-interacting motif 2). In contrast, little is known about the specificity or function of the domain from HYD. Here, we used isothermal calorimetry and surface plasmon resonance titrations to show that the PABC domain of HYD binds PAM2 peptides with micromolar affinity. NMR chemical shift perturbations were used to map the peptide-binding site in the PABC domain of HYD. The structural features of binding are very similar to those of the interactions with the domain of PABP, which explains the overlapping peptide specificity and binding affinity. We identified the anti-proliferative Tob proteins as potential binding partners of HYD. This was confirmed by glutathione S-transferase pulldown and immunoprecipitation experiments demonstrating the interaction with full-length Tob2. Altogether, our results point to a role of the PABC domain as a protein-protein interaction domain that brings together the processes of translation, ubiquitin-mediated protein degradation, and cell cycle control.

Received for publication, January 11, 2006 , and in revised form, March 7, 2006.

^* This work was supported in part by Canadian Institutes of Health Research Grant MA14219 (to K. G.) and National Institutes of Health Grant GM46454 (to A.-B. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 514-398-7287; Fax: 514-398-7384; E-mail: kalle.gehring{at}mcgill.ca.

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